FMO DATABASE

FMODB ID: N9ZMQ

Calculation Name: 1ORJ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1ORJ

Chain ID: A

ChEMBL ID:

UniProt ID: O67806

Base Structure: X-ray

Registration Date: 2023-06-22

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	126
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1148084.860579
FMO2-HF: Nuclear repulsion	1096404.563133
FMO2-HF: Total energy	-51680.297446
FMO2-MP2: Total energy	-51833.964677

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:1002:ARG)

Summations of interaction energy for fragment #1(A:1002:ARG)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-168.714	-169.148	19.5	-9.389	-9.676	-0.097

Interaction energy analysis for fragmet #1(A:1002:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.892 / q_NPA : 0.927

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

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Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	1004	ILE	0	0.103	0.059	3.816	-4.538	-2.711	-0.011	-0.822	-0.993	0.005
4	A	1005	ALA	0	0.047	0.016	5.816	2.322	2.322	0.000	0.000	0.000	0.000
5	A	1006	GLU	-1	-0.884	-0.926	4.999	-31.747	-31.747	0.000	0.000	0.000	0.000
6	A	1007	ALA	0	-0.042	-0.002	7.226	1.068	1.068	0.000	0.000	0.000	0.000
7	A	1008	TYR	0	0.001	-0.003	8.669	1.916	1.916	0.000	0.000	0.000	0.000
8	A	1009	PHE	0	-0.021	-0.007	10.665	1.739	1.739	0.000	0.000	0.000	0.000
9	A	1010	GLN	0	0.007	0.009	10.568	-1.917	-1.917	0.000	0.000	0.000	0.000
10	A	1011	ASN	0	-0.015	-0.039	7.947	2.394	2.394	0.000	0.000	0.000	0.000
11	A	1012	MET	0	-0.043	-0.013	10.849	-0.022	-0.022	0.000	0.000	0.000	0.000
12	A	1013	VAL	0	-0.038	-0.006	13.905	1.447	1.447	0.000	0.000	0.000	0.000
13	A	1014	GLU	-1	-0.832	-0.929	15.098	-15.568	-15.568	0.000	0.000	0.000	0.000
14	A	1015	THR	0	-0.080	-0.037	17.704	0.594	0.594	0.000	0.000	0.000	0.000
15	A	1016	ALA	0	0.053	0.016	17.885	-0.636	-0.636	0.000	0.000	0.000	0.000
16	A	1017	THR	0	0.023	0.018	18.936	-0.112	-0.112	0.000	0.000	0.000	0.000
17	A	1018	PRO	0	0.003	-0.012	17.500	0.176	0.176	0.000	0.000	0.000	0.000
18	A	1019	LEU	0	0.016	0.013	12.941	-0.277	-0.277	0.000	0.000	0.000	0.000
19	A	1020	GLU	-1	-0.860	-0.937	16.404	-13.288	-13.288	0.000	0.000	0.000	0.000
20	A	1021	GLN	0	0.019	0.013	18.974	0.405	0.405	0.000	0.000	0.000	0.000
21	A	1022	ILE	0	-0.027	-0.006	13.662	0.287	0.287	0.000	0.000	0.000	0.000
22	A	1023	ILE	0	0.012	0.003	14.523	0.029	0.029	0.000	0.000	0.000	0.000
23	A	1024	LEU	0	0.022	0.016	17.009	0.469	0.469	0.000	0.000	0.000	0.000
24	A	1025	LEU	0	-0.038	-0.003	18.865	0.460	0.460	0.000	0.000	0.000	0.000
25	A	1026	TYR	0	0.002	-0.028	12.435	-0.077	-0.077	0.000	0.000	0.000	0.000
26	A	1027	ASP	-1	-0.810	-0.886	18.101	-12.789	-12.789	0.000	0.000	0.000	0.000
27	A	1028	LYS	1	0.764	0.859	20.676	10.832	10.832	0.000	0.000	0.000	0.000
28	A	1029	ALA	0	0.013	-0.005	20.035	0.399	0.399	0.000	0.000	0.000	0.000
29	A	1030	ILE	0	-0.014	-0.008	17.069	0.212	0.212	0.000	0.000	0.000	0.000
30	A	1031	GLU	-1	-0.755	-0.848	21.540	-9.920	-9.920	0.000	0.000	0.000	0.000
31	A	1032	CYS	0	-0.056	-0.029	25.011	0.441	0.441	0.000	0.000	0.000	0.000
32	A	1033	LEU	0	0.008	-0.004	21.609	0.304	0.304	0.000	0.000	0.000	0.000
33	A	1034	GLU	-1	-0.824	-0.928	23.313	-11.151	-11.151	0.000	0.000	0.000	0.000
34	A	1035	ARG	1	0.773	0.857	26.296	8.772	8.772	0.000	0.000	0.000	0.000
35	A	1036	ALA	0	0.010	-0.002	28.139	0.301	0.301	0.000	0.000	0.000	0.000
36	A	1037	ILE	0	-0.027	-0.020	24.588	0.226	0.226	0.000	0.000	0.000	0.000
37	A	1038	GLU	-1	-0.936	-0.947	29.064	-8.470	-8.470	0.000	0.000	0.000	0.000
38	A	1039	ILE	0	-0.048	-0.029	31.592	0.321	0.321	0.000	0.000	0.000	0.000
39	A	1040	TYR	0	-0.035	-0.030	30.878	0.221	0.221	0.000	0.000	0.000	0.000
40	A	1041	ASP	-1	-0.859	-0.925	33.490	-8.395	-8.395	0.000	0.000	0.000	0.000
41	A	1042	GLN	0	-0.010	-0.002	36.491	0.296	0.296	0.000	0.000	0.000	0.000
42	A	1043	VAL	0	0.032	0.026	35.537	0.190	0.190	0.000	0.000	0.000	0.000
43	A	1044	ASN	0	-0.011	0.002	38.801	0.084	0.084	0.000	0.000	0.000	0.000
44	A	1045	GLU	-1	-0.818	-0.916	41.725	-6.887	-6.887	0.000	0.000	0.000	0.000
45	A	1046	LEU	0	-0.021	-0.005	41.553	-0.154	-0.154	0.000	0.000	0.000	0.000
46	A	1047	GLU	-1	-0.845	-0.912	41.922	-6.942	-6.942	0.000	0.000	0.000	0.000
47	A	1048	LYS	1	0.915	0.946	37.862	7.168	7.168	0.000	0.000	0.000	0.000
48	A	1049	ARG	1	0.878	0.929	36.990	7.087	7.087	0.000	0.000	0.000	0.000
49	A	1050	LYS	1	0.843	0.916	36.746	6.873	6.873	0.000	0.000	0.000	0.000
50	A	1051	GLU	-1	-0.733	-0.837	34.409	-8.490	-8.490	0.000	0.000	0.000	0.000
51	A	1052	PHE	0	-0.022	-0.005	30.864	-0.304	-0.304	0.000	0.000	0.000	0.000
52	A	1053	VAL	0	-0.018	-0.023	31.934	-0.288	-0.288	0.000	0.000	0.000	0.000
53	A	1054	GLU	-1	-0.844	-0.893	32.423	-8.433	-8.433	0.000	0.000	0.000	0.000
54	A	1055	ASN	0	-0.072	-0.051	29.276	-0.417	-0.417	0.000	0.000	0.000	0.000
55	A	1056	ILE	0	0.012	0.003	27.223	-0.444	-0.444	0.000	0.000	0.000	0.000
56	A	1057	ASP	-1	-0.908	-0.946	27.471	-9.809	-9.809	0.000	0.000	0.000	0.000
57	A	1058	ARG	1	0.834	0.916	27.456	8.829	8.829	0.000	0.000	0.000	0.000
58	A	1059	VAL	0	-0.019	-0.008	22.220	-0.434	-0.434	0.000	0.000	0.000	0.000
59	A	1060	TYR	0	0.008	0.004	22.941	-0.752	-0.752	0.000	0.000	0.000	0.000
60	A	1061	ASP	-1	-0.877	-0.939	23.884	-11.128	-11.128	0.000	0.000	0.000	0.000
61	A	1062	ILE	0	-0.062	-0.030	20.512	-0.399	-0.399	0.000	0.000	0.000	0.000
62	A	1063	ILE	0	-0.005	-0.007	17.630	-0.750	-0.750	0.000	0.000	0.000	0.000
63	A	1064	SER	0	-0.010	-0.010	19.153	-0.809	-0.809	0.000	0.000	0.000	0.000
64	A	1065	ALA	0	-0.032	0.003	20.783	-0.377	-0.377	0.000	0.000	0.000	0.000
65	A	1066	LEU	0	-0.020	-0.006	15.884	-0.585	-0.585	0.000	0.000	0.000	0.000
66	A	1067	LYS	1	0.847	0.896	15.976	15.959	15.959	0.000	0.000	0.000	0.000
67	A	1068	SER	0	-0.084	-0.056	16.660	-0.458	-0.458	0.000	0.000	0.000	0.000
68	A	1069	PHE	0	-0.059	-0.038	17.169	0.253	0.253	0.000	0.000	0.000	0.000
69	A	1070	LEU	0	-0.060	-0.010	11.181	-0.823	-0.823	0.000	0.000	0.000	0.000
70	A	1071	ASP	-1	-0.806	-0.898	11.764	-20.606	-20.606	0.000	0.000	0.000	0.000
71	A	1072	HIS	0	-0.038	-0.038	11.616	-2.002	-2.002	0.000	0.000	0.000	0.000
72	A	1073	GLU	-1	-0.902	-0.926	12.318	-18.938	-18.938	0.000	0.000	0.000	0.000
73	A	1074	LYS	1	0.807	0.886	11.448	18.014	18.014	0.000	0.000	0.000	0.000
74	A	1075	GLY	0	0.100	0.061	8.742	-1.999	-1.999	0.000	0.000	0.000	0.000
75	A	1076	LYS	1	0.739	0.854	5.148	30.354	30.354	0.000	0.000	0.000	0.000
76	A	1077	GLU	-1	-0.793	-0.904	1.692	-107.067	-109.986	17.576	-8.029	-6.628	-0.099
77	A	1078	ILE	0	-0.045	-0.009	2.351	0.414	1.072	1.935	-0.538	-2.055	-0.003
78	A	1079	ALA	0	0.091	0.051	5.435	4.057	4.057	0.000	0.000	0.000	0.000
79	A	1080	LYS	1	0.853	0.938	8.973	24.487	24.487	0.000	0.000	0.000	0.000
80	A	1081	ASN	0	-0.001	-0.021	5.780	6.127	6.127	0.000	0.000	0.000	0.000
81	A	1082	LEU	0	0.064	0.029	7.476	2.172	2.172	0.000	0.000	0.000	0.000
82	A	1083	ASP	-1	-0.792	-0.865	10.268	-17.038	-17.038	0.000	0.000	0.000	0.000
83	A	1084	THR	0	-0.074	-0.019	12.378	2.131	2.131	0.000	0.000	0.000	0.000
84	A	1085	ILE	0	0.038	0.022	9.675	1.489	1.489	0.000	0.000	0.000	0.000
85	A	1086	TYR	0	0.086	0.049	13.718	0.833	0.833	0.000	0.000	0.000	0.000
86	A	1087	THR	0	-0.036	-0.034	15.975	1.376	1.376	0.000	0.000	0.000	0.000
87	A	1088	ILE	0	-0.019	0.003	15.651	0.970	0.970	0.000	0.000	0.000	0.000
88	A	1089	ILE	0	0.031	0.024	15.893	0.938	0.938	0.000	0.000	0.000	0.000
89	A	1090	LEU	0	0.009	0.003	19.559	0.758	0.758	0.000	0.000	0.000	0.000
90	A	1091	ASN	0	-0.030	-0.028	21.738	0.845	0.845	0.000	0.000	0.000	0.000
91	A	1092	THR	0	-0.041	-0.024	21.789	0.555	0.555	0.000	0.000	0.000	0.000
92	A	1093	LEU	0	0.008	0.002	22.592	0.548	0.548	0.000	0.000	0.000	0.000
93	A	1094	VAL	0	0.004	0.015	25.779	0.541	0.541	0.000	0.000	0.000	0.000
94	A	1095	LYS	1	0.767	0.899	26.837	10.988	10.988	0.000	0.000	0.000	0.000
95	A	1096	VAL	0	-0.006	-0.012	29.470	0.111	0.111	0.000	0.000	0.000	0.000
96	A	1097	ASP	-1	-0.905	-0.937	31.353	-9.483	-9.483	0.000	0.000	0.000	0.000
97	A	1098	LYS	1	0.818	0.913	28.088	9.979	9.979	0.000	0.000	0.000	0.000
98	A	1099	THR	0	0.011	-0.004	28.480	0.297	0.297	0.000	0.000	0.000	0.000
99	A	1100	LYS	1	0.841	0.898	28.078	8.775	8.775	0.000	0.000	0.000	0.000
100	A	1101	GLU	-1	-0.829	-0.898	25.715	-11.419	-11.419	0.000	0.000	0.000	0.000
101	A	1102	GLU	-1	-0.768	-0.872	23.963	-11.533	-11.533	0.000	0.000	0.000	0.000
102	A	1103	LEU	0	0.026	-0.001	22.889	-0.512	-0.512	0.000	0.000	0.000	0.000
103	A	1104	GLN	0	0.011	-0.004	22.915	-0.015	-0.015	0.000	0.000	0.000	0.000
104	A	1105	LYS	1	0.858	0.921	20.016	11.892	11.892	0.000	0.000	0.000	0.000
105	A	1106	ILE	0	0.012	0.014	18.510	-0.648	-0.648	0.000	0.000	0.000	0.000
106	A	1107	LEU	0	-0.027	0.001	18.030	-0.587	-0.587	0.000	0.000	0.000	0.000
107	A	1108	GLU	-1	-0.882	-0.943	17.510	-13.358	-13.358	0.000	0.000	0.000	0.000
108	A	1109	ILE	0	-0.014	0.002	13.120	-0.539	-0.539	0.000	0.000	0.000	0.000
109	A	1110	LEU	0	-0.039	-0.017	13.634	-0.838	-0.838	0.000	0.000	0.000	0.000
110	A	1111	LYS	1	0.835	0.923	14.692	11.944	11.944	0.000	0.000	0.000	0.000
111	A	1112	ASP	-1	-0.892	-0.963	10.013	-21.254	-21.254	0.000	0.000	0.000	0.000
112	A	1113	LEU	0	-0.020	0.000	8.974	-1.168	-1.168	0.000	0.000	0.000	0.000
113	A	1114	ARG	1	0.832	0.895	10.670	13.333	13.333	0.000	0.000	0.000	0.000
114	A	1115	GLU	-1	-0.958	-0.974	11.636	-17.682	-17.682	0.000	0.000	0.000	0.000
115	A	1116	ALA	0	0.016	0.007	6.746	-0.535	-0.535	0.000	0.000	0.000	0.000
116	A	1117	TRP	0	-0.038	-0.032	8.719	-1.254	-1.254	0.000	0.000	0.000	0.000
117	A	1118	GLU	-1	-0.868	-0.945	10.923	-14.480	-14.480	0.000	0.000	0.000	0.000
118	A	1119	GLU	-1	-0.803	-0.884	8.360	-22.848	-22.848	0.000	0.000	0.000	0.000
119	A	1120	VAL	0	-0.030	-0.018	7.787	-0.654	-0.654	0.000	0.000	0.000	0.000
120	A	1121	LYS	1	0.902	0.947	10.243	14.768	14.768	0.000	0.000	0.000	0.000
121	A	1122	LYS	1	0.925	0.976	13.181	17.523	17.523	0.000	0.000	0.000	0.000
122	A	1123	LYS	1	0.714	0.826	6.539	25.450	25.450	0.000	0.000	0.000	0.000
123	A	1124	VAL	0	-0.001	0.007	12.075	0.203	0.203	0.000	0.000	0.000	0.000
124	A	1125	HIS	0	0.029	0.019	14.225	0.273	0.273	0.000	0.000	0.000	0.000
125	A	1126	HIS	0	-0.124	-0.054	15.590	0.889	0.889	0.000	0.000	0.000	0.000
126	A	1127	HIS	0	-0.022	0.013	14.635	0.225	0.225	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1002:ARG)